chaperonin

(redirected from Chaperonins)
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chap·er·o·nin

 (shăp′ə-rō′nĭn)
n.
Any of a family of large chaperone proteins that function chiefly to assist in the folding of newly synthesized proteins.

References in periodicals archive ?
They found a well-defined pattern in chaperonins HSPs and ORP150 (osteogenetic regulatory protein) over time expression; they concluded that positivity for both HSP70 and ORP150 is consistently associated with a lag time from the insult of less than 8 hours, while HSP90 turns positive only after this time span until about 48 hours.
Among these, one gene (hvpepc4) encoded the C4 photosynthetic PEPC (phosphoenolpyruvate carboxylase) (which was substantially upregulated especially in the light), two encoded distinct isoforms of PPDK (pyruvate orthophosphate dikinase), and genes encoding an aminotransferase, a transporter, and two chaperonins were also upregulated.
Xenorhabdus bacteria also produce another insecticidal protein called HIP57 that is similar to chaperonins like GroEL produce by E.
Until now little information is known about the relationships between GRSP and root carbohydrates.Since GRSP may be located in hyphae surfaces and spore wells of AMF but also in surfaces of roots and soil aggregates Purin and Rillig (2007) postulated a primary cellular function of GRSP in fungal physiology such as chaperonins and a secondarily environmental function of GRSP in aggregate stability.
Cohen, "Autoimmunity to chaperonins in the pathogenesis of arthritis and diabetes," Annual Review of Immunology, vol.
Admittedly, things haven't turned out to be quite that simple, and there is a whole class of proteins called "chaperonins" that guide folding and prevent unwanted interactions, as this metaphorical name implies (Ranson et al., 2008).
Further, spots 11 and 12 (Rv3418c) encodes 10 kDa chaperonin. Chaperonins form a sub-group of molecular chaperones and 10-kDa antigen has homology with the GroES or chaperonin-10 (Cpn l0) family of heat shock proteins (17-19).
In vitro as well as in vivo chaperonins, either alone or with other chaperones and ATP, have been shown to orchestrate the re-folding of partially denatured proteins.
Chaperonins, which assist in the assembly-disassembly of proteins in the cytoplasm such as the phenylpropanoid pathway enzyme complex, may be another function associated with these QTL (Dr.
In general, treatment with these chemicals agents led to the up-regulation of liver proteins involved in detoxification or response to stress, such as catalase, glutathione peroxidase, sulfotransferases, serine proteinase inhibitor, heat shock proteins or chaperonins, and glutathione S-transferase.
These interactions include 148 ribosomal complex interactions and 163 degradosomal complex interactions (typically involving chaperonins), systems that are critical to cellular function.